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{{AE}} Henry A. Hoff
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''Serum response factor''', also known as '''SRF''', is a [[transcription factor|transcription factor protein]].<ref name="pmid3203386">{{cite journal | vauthors = Norman C, Runswick M, Pollock R, Treisman R | title = Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element | journal = Cell | volume = 55 | issue = 6 | pages = 989–1003  | date = December 1988 | pmid = 3203386 | doi = 10.1016/0092-8674(88)90244-9 }}</ref>
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = no
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_SRF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hbx.
| PDB = {{PDB2|1hbx}}, {{PDB2|1k6o}}, {{PDB2|1srs}}
| Name = Serum response factor (c-fos serum response element-binding transcription factor)
| HGNCid = 11291
| Symbol = SRF
| AltSymbols =; MCM1
| OMIM = 600589
| ECnumber = 
| Homologene = 31135
| MGIid = 106658
| GeneAtlas_image1 = PBB_GE_SRF_202401_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SRF_202400_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001947 |text = heart looping}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0046716 |text = muscle maintenance}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6722
    | Hs_Ensembl = ENSG00000112658
    | Hs_RefseqProtein = NP_003122
    | Hs_RefseqmRNA = NM_003131
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 43246898
    | Hs_GenLoc_end = 43257219
    | Hs_Uniprot = P11831
    | Mm_EntrezGene = 20807
    | Mm_Ensembl = ENSMUSG00000015605
    | Mm_RefseqmRNA = NM_020493
    | Mm_RefseqProtein = NP_065239
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 46010028
    | Mm_GenLoc_end = 46019351
    | Mm_Uniprot = Q9JM73
  }}
}}
'''Serum response factor (c-fos serum response element-binding transcription factor)''', also known as '''SRF''', is a [[transcription factor]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Gene ID: 6722 SRF serum response factor, "This gene encodes a ubiquitous nuclear protein that stimulates both cell proliferation and differentiation. It is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors. This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate-early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs). Two transcript variants encoding different isoforms have been found for this gene."<ref name=RefSeq>{{ cite web
{{PBB_Summary
|author=RefSeq
| section_title =
|title=SRF serum response factor [ Homo sapiens (human) ]
| summary_text = It is a member of the [[MADS-box | MADS (MCM1, Agamous, Deficiens, and SRF) box]] superfamily of transcription factors. This protein binds to the [[serum response element]] (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate-early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs).<ref>{{cite web | title = Entrez Gene: SRF serum response factor (c-fos serum response element-binding transcription factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6722| accessdate = }}</ref>
|publisher=National Center for Biotechnology Information, U.S. National Library of Medicine
}}
|location=8600 Rockville Pike, Bethesda MD, 20894 USA
|date=May 2014
|url=https://www.ncbi.nlm.nih.gov/gene/6722
|accessdate=23 November 2019 }}</ref>
# NP_003122.1 serum response factor isoform 1: "This variant (1) represents the longer transcript and encodes the longer isoform (1)."<ref name=RefSeq/> cd00266 (Location:142 → 223): "MADS_SRF_like; SRF-like/Type I subfamily of MADS (MCM1, Agamous, Deficiens, and SRF (serum response factor) box family of eukaryotic transcriptional regulators. Binds DNA and exists as hetero- and homo-dimers. Differs from the MEF-like/Type II subgroup mainly in position of the alpha 2 helix responsible for the dimerization interface. Important in homeotic regulation in plants and in immediate-early development in animals. Also found in fungi."<ref name=Cd00266>{{ cite web
|author=cd00266
|title=Conserved Protein Domain Family MADS_SRF_like
|publisher=National Center for Biotechnology Information, U.S. National Library of Medicine
|location=8600 Rockville Pike, Bethesda MD, 20894 USA
|date=17 January 2013
|url=https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=238166
|accessdate=23 November 2019 }}</ref>
# NP_001278930.1 serum response factor isoform 2: "This variant (2) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (2) is shorter at the N-terminus compared to isoform 1."<ref name=RefSeq/>


==References==
Serum response factor is a member of the [[MADS-box|MADS]] ('''M'''CM1, '''A'''gamous, '''D'''eficiens, and '''S'''RF) box superfamily of transcription factors.<ref name="pmid7744019">{{cite journal | vauthors = Shore P, Sharrocks AD | title = The MADS-box family of transcription factors | journal = Eur. J. Biochem. | volume = 229 | issue = 1 | pages = 1–13 | date = April 1995 | pmid = 7744019 | doi = 10.1111/j.1432-1033.1995.0001l.x }}</ref> This protein binds to the serum response element (SRE) in the [[promotor (biology)|promoter]] region of target genes. This protein regulates the activity of many [[immediate early genes]], for example [[c-fos]], and thereby participates in [[cell cycle]] regulation, [[apoptosis]], cell growth, and [[cellular differentiation|cell differentiation]]. This gene is the downstream target of many pathways; for example, the [[mitogen-activated protein kinase]] pathway (MAPK) that acts through the ternary complex factors (TCFs).<ref name="pmid8103935">{{cite journal | vauthors = Dalton S, Marais R, Wynne J, Treisman R | title = Isolation and characterization of SRF accessory proteins | journal = Philos. Trans. R. Soc. Lond. B Biol. Sci. | volume = 340 | issue = 1293 | pages = 325–32  | date = June 1993 | pmid = 8103935 | doi = 10.1098/rstb.1993.0074 }}</ref><ref name="urlGene Result">{{cite web | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6722 | title = SRF serum response factor | author = | authorlink = | format = | work = Entrez Gene | publisher = National Center for Biotechnology Information, National Institutes of Health| pages = | archiveurl = | archivedate = | quote = | accessdate = }}</ref>
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Miano JM |title=Serum response factor: toggling between disparate programs of gene expression. |journal=J. Mol. Cell. Cardiol. |volume=35 |issue= 6 |pages= 577-93 |year= 2004 |pmid= 12788374 |doi=  }}
*{{cite journal  | author=Reason AJ, Morris HR, Panico M, ''et al.'' |title=Localization of O-GlcNAc modification on the serum response transcription factor. |journal=J. Biol. Chem. |volume=267 |issue= 24 |pages= 16911-21 |year= 1992 |pmid= 1512232 |doi=  }}
*{{cite journal  | author=Janknecht R, Hipskind RA, Houthaeve T, ''et al.'' |title=Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties. |journal=EMBO J. |volume=11 |issue= 3 |pages= 1045-54 |year= 1992 |pmid= 1547771 |doi=  }}
*{{cite journal  | author=Marais RM, Hsuan JJ, McGuigan C, ''et al.'' |title=Casein kinase II phosphorylation increases the rate of serum response factor-binding site exchange. |journal=EMBO J. |volume=11 |issue= 1 |pages= 97-105 |year= 1992 |pmid= 1740119 |doi=  }}
*{{cite journal | author=Manak JR, Prywes R |title=Mutation of serum response factor phosphorylation sites and the mechanism by which its DNA-binding activity is increased by casein kinase II. |journal=Mol. Cell. Biol. |volume=11 |issue= 7 |pages= 3652-9 |year= 1991 |pmid= 2046671 |doi=  }}
*{{cite journal  | author=Norman C, Runswick M, Pollock R, Treisman R |title=Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element. |journal=Cell |volume=55 |issue= 6 |pages= 989-1003 |year= 1989 |pmid= 3203386 |doi=  }}
*{{cite journal  | author=Price MA, Rogers AE, Treisman R |title=Comparative analysis of the ternary complex factors Elk-1, SAP-1a and SAP-2 (ERP/NET). |journal=EMBO J. |volume=14 |issue= 11 |pages= 2589-601 |year= 1995 |pmid= 7540136 |doi=  }}
*{{cite journal | author=Bonni A, Ginty DD, Dudek H, Greenberg ME |title=Serine 133-phosphorylated CREB induces transcription via a cooperative mechanism that may confer specificity to neurotrophin signals. |journal=Mol. Cell. Neurosci. |volume=6 |issue= 2 |pages= 168-83 |year= 1995 |pmid= 7551568 |doi= 10.1006/mcne.1995.1015 }}
*{{cite journal  | author=Fujii M, Chuhjo T, Minamino T, ''et al.'' |title=Identification of the Tax interaction region of serum response factor that mediates the aberrant induction of immediate early genes through CArG boxes by HTLV-I Tax. |journal=Oncogene |volume=11 |issue= 1 |pages= 7-14 |year= 1995 |pmid= 7624133 |doi=  }}
*{{cite journal  | author=Pellegrini L, Tan S, Richmond TJ |title=Structure of serum response factor core bound to DNA. |journal=Nature |volume=376 |issue= 6540 |pages= 490-8 |year= 1995 |pmid= 7637780 |doi= 10.1038/376490a0 }}
*{{cite journal  | author=Liu SH, Peng BH, Ma JT, ''et al.'' |title=Serum response element associated transcription factors in mouse embryos: serum response factor, YY1, and PEA3 factor. |journal=Dev. Genet. |volume=16 |issue= 3 |pages= 229-40 |year= 1995 |pmid= 7796532 |doi= 10.1002/dvg.1020160303 }}
*{{cite journal  | author=Joliot V, Demma M, Prywes R |title=Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor. |journal=Nature |volume=373 |issue= 6515 |pages= 632-5 |year= 1995 |pmid= 7854423 |doi= 10.1038/373632a0 }}
*{{cite journal  | author=Liu SH, Ng SY |title=Serum response factor associated ETS proteins: ternary complex factors and PEA3-binding factor. |journal=Biochem. Biophys. Res. Commun. |volume=201 |issue= 3 |pages= 1406-13 |year= 1994 |pmid= 8024585 |doi= 10.1006/bbrc.1994.1860 }}
*{{cite journal | author=Zhu H, Joliot V, Prywes R |title=Role of transcription factor TFIIF in serum response factor-activated transcription. |journal=J. Biol. Chem. |volume=269 |issue= 5 |pages= 3489-97 |year= 1994 |pmid= 8106390 |doi=  }}
*{{cite journal  | author=Janknecht R, Ernst WH, Houthaeve T, Nordheim A |title=C-terminal phosphorylation of the serum-response factor. |journal=Eur. J. Biochem. |volume=216 |issue= 2 |pages= 469-75 |year= 1993 |pmid= 8375385 |doi= }}
*{{cite journal  | author=Liu SH, Ma JT, Yueh AY, ''et al.'' |title=The carboxyl-terminal transactivation domain of human serum response factor contains DNA-activated protein kinase phosphorylation sites. |journal=J. Biol. Chem. |volume=268 |issue= 28 |pages= 21147-54 |year= 1993 |pmid= 8407951 |doi=  }}
*{{cite journal  | author=Rivera VM, Miranti CK, Misra RP, ''et al.'' |title=A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity. |journal=Mol. Cell. Biol. |volume=13 |issue= 10 |pages= 6260-73 |year= 1993 |pmid= 8413226 |doi=  }}
*{{cite journal  | author=Magnaghi-Jaulin L, Masutani H, Robin P, ''et al.'' |title=SRE elements are binding sites for the fusion protein EWS-FLI-1. |journal=Nucleic Acids Res. |volume=24 |issue= 6 |pages= 1052-8 |year= 1996 |pmid= 8604338 |doi=  }}
*{{cite journal  | author=Groisman R, Masutani H, Leibovitch MP, ''et al.'' |title=Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins. |journal=J. Biol. Chem. |volume=271 |issue= 9 |pages= 5258-64 |year= 1996 |pmid= 8617811 |doi=  }}
*{{cite journal  | author=Franzoso G, Carlson L, Brown K, ''et al.'' |title=Activation of the serum response factor by p65/NF-kappaB. |journal=EMBO J. |volume=15 |issue= 13 |pages= 3403-12 |year= 1996 |pmid= 8670842 |doi= }}
}}
{{refend}}


{{protein-stub}}
SRF is important during the development of the embryo, as it has been linked to the formation of [[mesoderm]].<ref name="pmid11983708">{{cite journal | vauthors = Sepulveda JL, Vlahopoulos S, Iyer D, Belaguli N, Schwartz RJ | title = Combinatorial expression of GATA4, Nkx2-5, and serum response factor directs early cardiac gene activity | journal = J. Biol. Chem. | volume = 277 | issue = 28 | pages = 25775–82  | date = July 2002 | pmid = 11983708 | doi = 10.1074/jbc.M203122200 }}</ref><ref name="pmid15591049">{{cite journal | vauthors = Barron MR, Belaguli NS, Zhang SX, Trinh M, Iyer D, Merlo X, Lough JW, Parmacek MS, Bruneau BG, Schwartz RJ | title = Serum response factor, an enriched cardiac mesoderm obligatory factor, is a downstream gene target for Tbx genes | journal = J. Biol. Chem. | volume = 280 | issue = 12 | pages = 11816–28  | date = March 2005 | pmid = 15591049 | doi = 10.1074/jbc.M412408200 }}</ref> In the fully developed mammal, SRF is crucial for the growth of skeletal muscle.<ref name="pmid15647354">{{cite journal | vauthors = Li S, Czubryt MP, McAnally J, Bassel-Duby R, Richardson JA, Wiebel FF, Nordheim A, Olson EN | title = Requirement for serum response factor for skeletal muscle growth and maturation revealed by tissue-specific gene deletion in mice | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 102 | issue = 4 | pages = 1082–7  | date = January 2005 | pmid = 15647354 | pmc = 545866 | doi = 10.1073/pnas.0409103102 }}</ref> Interaction of SRF with other proteins, such as [[steroid hormone receptor]]s, may contribute to regulation of muscle growth by [[steroid]]s.<ref name="pmid15623502">{{cite journal | vauthors = Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ | title = Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene | journal = J. Biol. Chem. | volume = 280 | issue = 9 | pages = 7786–92  | date = March 2005 | pmid = 15623502 | doi = 10.1074/jbc.M413992200 }}</ref> Interaction of SRF with other proteins such as myocardin or Elk-1 may enhance or suppress expression of genes important for growth of vascular smooth muscle.
{{Transcription factors}}
 
==Transcriptions==
 
"A common feature of many muscle genes is their dependence on a ''cis''-acting sequence known as a CArG box (CC(A/T)<sub>6</sub>GG), which serves as the binding site for serum response factor (SRF) (reviewed in Shore and Sharrocks, 1995)."<ref name=Wang>{{ cite journal
|author=Da-Zhi Wang, Priscilla S. Chang, Zhigao Wang, Lillian Sutherland, James A. Richardson, Eric Small, Paul A. Krieg and Eric N. Olson
|title=Activation of cardiac gene expression by myocardin, a transcriptional cofactor for serum response factor
|journal=Cell
|date=29 June 2001
|volume=105
|issue=7
|pages=851-862
|url=https://www.sciencedirect.com/science/article/pii/S0092867401004044
|arxiv=
|bibcode=
|doi=10.1016/S0092-8674(01)00404-4
|pmid=
|accessdate=26 November 2019 }}</ref>
 
== Interactions ==
 
Serum response factor has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[ASCC3]],<ref name = pmid12077347>{{cite journal | vauthors = Jung DJ, Sung HS, Goo YW, Lee HM, Park OK, Jung SY, Lim J, Kim HJ, Lee SK, Kim TS, Lee JW, Lee YC | title = Novel transcription coactivator complex containing activating signal cointegrator 1 | journal = Mol. Cell. Biol. | volume = 22 | issue = 14 | pages = 5203–11  | date = July 2002 | pmid = 12077347 | pmc = 139772 | doi =  10.1128/mcb.22.14.5203-5211.2002}}</ref>
* [[ATF6]],<ref name = pmid9271374>{{cite journal | vauthors = Zhu C, Johansen FE, Prywes R | title = Interaction of ATF6 and serum response factor | journal = Mol. Cell. Biol. | volume = 17 | issue = 9 | pages = 4957–66  | date = September 1997 | pmid = 9271374 | pmc = 232347 | doi =  }}</ref>
* [[CEBPB]],<ref name = pmid10318842>{{cite journal | vauthors = Hanlon M, Sealy L | title = Ras regulates the association of serum response factor and CCAAT/enhancer-binding protein beta | journal = J. Biol. Chem. | volume = 274 | issue = 20 | pages = 14224–8  | date = May 1999 | pmid = 10318842 | doi =  10.1074/jbc.274.20.14224}}</ref><ref name = pmid9032301>{{cite journal | vauthors = Sealy L, Malone D, Pawlak M | title = Regulation of the cfos serum response element by C/EBPbeta | journal = Mol. Cell. Biol. | volume = 17 | issue = 3 | pages = 1744–55  | date = March 1997 | pmid = 9032301 | pmc = 231899 | doi =  10.1128/mcb.17.3.1744}}</ref>
* [[CREB-binding protein]],<ref name = pmid12622724>{{cite journal | vauthors = Matsuzaki K, Minami T, Tojo M, Honda Y, Saitoh N, Nagahiro S, Saya H, Nakao M | title = PML-nuclear bodies are involved in cellular serum response | journal = Genes Cells | volume = 8 | issue = 3 | pages = 275–86  | date = March 2003 | pmid = 12622724 | doi =  10.1046/j.1365-2443.2003.00632.x}}</ref>
* [[ELK4]],<ref name = pmid9271374/><ref name = pmid11406578>{{cite journal | vauthors = Hassler M, Richmond TJ | title = The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex | journal = EMBO J. | volume = 20 | issue = 12 | pages = 3018–28  | date = June 2001 | pmid = 11406578 | pmc = 150215 | doi = 10.1093/emboj/20.12.3018 }}</ref>
* [[GATA4]],<ref name = pmid11003651>{{cite journal | vauthors = Belaguli NS, Sepulveda JL, Nigam V, Charron F, Nemer M, Schwartz RJ | title = Cardiac tissue enriched factors serum response factor and GATA-4 are mutual coregulators | journal = Mol. Cell. Biol. | volume = 20 | issue = 20 | pages = 7550–8  | date = October 2000 | pmid = 11003651 | pmc = 86307 | doi =  10.1128/mcb.20.20.7550-7558.2000}}</ref><ref name = pmid11158291>{{cite journal | vauthors = Morin S, Paradis P, Aries A, Nemer M | title = Serum response factor-GATA ternary complex required for nuclear signaling by a G-protein-coupled receptor | journal = Mol. Cell. Biol. | volume = 21 | issue = 4 | pages = 1036–44  | date = February 2001 | pmid = 11158291 | pmc = 99558 | doi = 10.1128/MCB.21.4.1036-1044.2001 }}</ref>
* [[GTF2F1]],<ref name = pmid7854423>{{cite journal | vauthors = Joliot V, Demma M, Prywes R | title = Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor | journal = Nature | volume = 373 | issue = 6515 | pages = 632–5  | date = February 1995 | pmid = 7854423 | doi = 10.1038/373632a0 }}</ref><ref name = pmid8106390>{{cite journal | vauthors = Zhu H, Joliot V, Prywes R | title = Role of transcription factor TFIIF in serum response factor-activated transcription | journal = J. Biol. Chem. | volume = 269 | issue = 5 | pages = 3489–97  | date = February 1994 | pmid = 8106390 | doi =  }}</ref>
* [[GTF2I]],<ref name = pmid9334314>{{cite journal | vauthors = Grueneberg DA, Henry RW, Brauer A, Novina CD, Cheriyath V, Roy AL, Gilman M | title = A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I | journal = Genes Dev. | volume = 11 | issue = 19 | pages = 2482–93  | date = October 1997 | pmid = 9334314 | pmc = 316568 | doi =  10.1101/gad.11.19.2482}}</ref><ref name = pmid9584171>{{cite journal | vauthors = Kim DW, Cheriyath V, Roy AL, Cochran BH | title = TFII-I enhances activation of the c-fos promoter through interactions with upstream elements | journal = Mol. Cell. Biol. | volume = 18 | issue = 6 | pages = 3310–20  | date = June 1998 | pmid = 9584171 | pmc = 108912 | doi =  10.1128/mcb.18.6.3310}}</ref>
* [[Myogenin]],<ref name = pmid8617811>{{cite journal | vauthors = Groisman R, Masutani H, Leibovitch MP, Robin P, Soudant I, Trouche D, Harel-Bellan A | title = Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins | journal = J. Biol. Chem. | volume = 271 | issue = 9 | pages = 5258–64  | date = March 1996 | pmid = 8617811 | doi =  10.1074/jbc.271.9.5258}}</ref><ref name = pmid10082523>{{cite journal | vauthors = Biesiada E, Hamamori Y, Kedes L, Sartorelli V | title = Myogenic basic helix-loop-helix proteins and Sp1 interact as components of a multiprotein transcriptional complex required for activity of the human cardiac alpha-actin promoter | journal = Mol. Cell. Biol. | volume = 19 | issue = 4 | pages = 2577–84  | date = April 1999 | pmid = 10082523 | pmc = 84050 | doi =  }}</ref>
* [[NFYA]],<ref name = pmid10571058>{{cite journal | vauthors = Yamada K, Osawa H, Granner DK | title = Identification of proteins that interact with NF-YA | journal = FEBS Lett. | volume = 460 | issue = 1 | pages = 41–5  | date = October 1999 | pmid = 10571058 | doi =  10.1016/s0014-5793(99)01311-3}}</ref>
* [[Nuclear receptor co-repressor 2]],<ref name = pmid10777532>{{cite journal | vauthors = Lee SK, Kim JH, Lee YC, Cheong J, Lee JW | title = Silencing mediator of retinoic acid and thyroid hormone receptors, as a novel transcriptional corepressor molecule of activating protein-1, nuclear factor-kappaB, and serum response factor | journal = J. Biol. Chem. | volume = 275 | issue = 17 | pages = 12470–4  | date = April 2000 | pmid = 10777532 | doi =  10.1074/jbc.275.17.12470}}</ref>
* [[Promyelocytic leukemia protein]]<ref name = pmid12622724/> and
* [[Src (gene)|Src]],<ref name = pmid9786846>{{cite journal | vauthors = Kim HJ, Kim JH, Lee JW | title = Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations | journal = J. Biol. Chem. | volume = 273 | issue = 44 | pages = 28564–7  | date = October 1998 | pmid = 9786846 | doi =  10.1074/jbc.273.44.28564}}</ref>  and
* [[TEAD1]].<ref name = pmid11136726>{{cite journal | vauthors = Gupta M, Kogut P, Davis FJ, Belaguli NS, Schwartz RJ, Gupta MP | title = Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1 | journal = J. Biol. Chem. | volume = 276 | issue = 13 | pages = 10413–22  | date = March 2001 | pmid = 11136726 | doi = 10.1074/jbc.M008625200 }}</ref>
{{Div col end}}
 
== Clinical significance ==
 
Lack of skin SRF is associated with [[psoriasis]] and other skin diseases.<ref name="pmid19307725">{{cite journal | vauthors = Koegel H, von Tobel L, Schäfer M, Alberti S, Kremmer E, Mauch C, Hohl D, Wang XJ, Beer HD, Bloch W, Nordheim A, Werner S | title = Loss of serum response factor in keratinocytes results in hyperproliferative skin disease in mice | journal = J. Clin. Invest. | volume = 119 | issue = 4 | pages = 899–910  | date = April 2009 | pmid = 19307725 | pmc = 2662566 | doi = 10.1172/JCI37771 }}</ref>
 
== References ==
{{Reflist|2}}
 
==Acknowledgements==
 
Initial content for this page in some instances incorporates text from the [https://www.ncbi.nlm.nih.gov/gene/6722 United States National Library of Medicine].
 
== External links ==
* {{MeshName|Serum+Response+Factor}}
* {{FactorBook|SRF}}
 
{{PDB_Gallery|geneid=6722}}
{{Transcription factors|g4}}
 
{{DEFAULTSORT:Serum Response Factor}}
[[Category:Resources last modified in November 2019]]
[[Category:Transcription factors]]
[[Category:Transcription factors]]
[[de:Serum-Response-Faktor]]
{{WikiDoc Sources}}

Latest revision as of 19:48, 11 January 2020

Associate Editor(s)-in-Chief: Henry A. Hoff

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Serum response factor, also known as SRF, is a transcription factor protein.[1]

Function

Gene ID: 6722 SRF serum response factor, "This gene encodes a ubiquitous nuclear protein that stimulates both cell proliferation and differentiation. It is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors. This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate-early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs). Two transcript variants encoding different isoforms have been found for this gene."[2]

  1. NP_003122.1 serum response factor isoform 1: "This variant (1) represents the longer transcript and encodes the longer isoform (1)."[2] cd00266 (Location:142 → 223): "MADS_SRF_like; SRF-like/Type I subfamily of MADS (MCM1, Agamous, Deficiens, and SRF (serum response factor) box family of eukaryotic transcriptional regulators. Binds DNA and exists as hetero- and homo-dimers. Differs from the MEF-like/Type II subgroup mainly in position of the alpha 2 helix responsible for the dimerization interface. Important in homeotic regulation in plants and in immediate-early development in animals. Also found in fungi."[3]
  2. NP_001278930.1 serum response factor isoform 2: "This variant (2) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (2) is shorter at the N-terminus compared to isoform 1."[2]

Serum response factor is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors.[4] This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs).[5][6]

SRF is important during the development of the embryo, as it has been linked to the formation of mesoderm.[7][8] In the fully developed mammal, SRF is crucial for the growth of skeletal muscle.[9] Interaction of SRF with other proteins, such as steroid hormone receptors, may contribute to regulation of muscle growth by steroids.[10] Interaction of SRF with other proteins such as myocardin or Elk-1 may enhance or suppress expression of genes important for growth of vascular smooth muscle.

Transcriptions

"A common feature of many muscle genes is their dependence on a cis-acting sequence known as a CArG box (CC(A/T)6GG), which serves as the binding site for serum response factor (SRF) (reviewed in Shore and Sharrocks, 1995)."[11]

Interactions

Serum response factor has been shown to interact with:

Clinical significance

Lack of skin SRF is associated with psoriasis and other skin diseases.[30]

References

  1. ↑ Norman C, Runswick M, Pollock R, Treisman R (December 1988). "Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element". Cell. 55 (6): 989–1003. doi:10.1016/0092-8674(88)90244-9. PMID 3203386.
  2. ↑ 2.0 2.1 2.2 RefSeq (May 2014). "SRF serum response factor [ Homo sapiens (human) ]". 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 23 November 2019.
  3. ↑ cd00266 (17 January 2013). "Conserved Protein Domain Family MADS_SRF_like". 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 23 November 2019.
  4. ↑ Shore P, Sharrocks AD (April 1995). "The MADS-box family of transcription factors". Eur. J. Biochem. 229 (1): 1–13. doi:10.1111/j.1432-1033.1995.0001l.x. PMID 7744019.
  5. ↑ Dalton S, Marais R, Wynne J, Treisman R (June 1993). "Isolation and characterization of SRF accessory proteins". Philos. Trans. R. Soc. Lond. B Biol. Sci. 340 (1293): 325–32. doi:10.1098/rstb.1993.0074. PMID 8103935.
  6. ↑ "SRF serum response factor". Entrez Gene. National Center for Biotechnology Information, National Institutes of Health.
  7. ↑ Sepulveda JL, Vlahopoulos S, Iyer D, Belaguli N, Schwartz RJ (July 2002). "Combinatorial expression of GATA4, Nkx2-5, and serum response factor directs early cardiac gene activity". J. Biol. Chem. 277 (28): 25775–82. doi:10.1074/jbc.M203122200. PMID 11983708.
  8. ↑ Barron MR, Belaguli NS, Zhang SX, Trinh M, Iyer D, Merlo X, Lough JW, Parmacek MS, Bruneau BG, Schwartz RJ (March 2005). "Serum response factor, an enriched cardiac mesoderm obligatory factor, is a downstream gene target for Tbx genes". J. Biol. Chem. 280 (12): 11816–28. doi:10.1074/jbc.M412408200. PMID 15591049.
  9. ↑ Li S, Czubryt MP, McAnally J, Bassel-Duby R, Richardson JA, Wiebel FF, Nordheim A, Olson EN (January 2005). "Requirement for serum response factor for skeletal muscle growth and maturation revealed by tissue-specific gene deletion in mice". Proc. Natl. Acad. Sci. U.S.A. 102 (4): 1082–7. doi:10.1073/pnas.0409103102. PMC 545866. PMID 15647354.
  10. ↑ Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ (March 2005). "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene". J. Biol. Chem. 280 (9): 7786–92. doi:10.1074/jbc.M413992200. PMID 15623502.
  11. ↑ Da-Zhi Wang, Priscilla S. Chang, Zhigao Wang, Lillian Sutherland, James A. Richardson, Eric Small, Paul A. Krieg and Eric N. Olson (29 June 2001). "Activation of cardiac gene expression by myocardin, a transcriptional cofactor for serum response factor". Cell. 105 (7): 851–862. doi:10.1016/S0092-8674(01)00404-4. Retrieved 26 November 2019.
  12. ↑ Jung DJ, Sung HS, Goo YW, Lee HM, Park OK, Jung SY, Lim J, Kim HJ, Lee SK, Kim TS, Lee JW, Lee YC (July 2002). "Novel transcription coactivator complex containing activating signal cointegrator 1". Mol. Cell. Biol. 22 (14): 5203–11. doi:10.1128/mcb.22.14.5203-5211.2002. PMC 139772. PMID 12077347.
  13. ↑ 13.0 13.1 Zhu C, Johansen FE, Prywes R (September 1997). "Interaction of ATF6 and serum response factor". Mol. Cell. Biol. 17 (9): 4957–66. PMC 232347. PMID 9271374.
  14. ↑ Hanlon M, Sealy L (May 1999). "Ras regulates the association of serum response factor and CCAAT/enhancer-binding protein beta". J. Biol. Chem. 274 (20): 14224–8. doi:10.1074/jbc.274.20.14224. PMID 10318842.
  15. ↑ Sealy L, Malone D, Pawlak M (March 1997). "Regulation of the cfos serum response element by C/EBPbeta". Mol. Cell. Biol. 17 (3): 1744–55. doi:10.1128/mcb.17.3.1744. PMC 231899. PMID 9032301.
  16. ↑ 16.0 16.1 Matsuzaki K, Minami T, Tojo M, Honda Y, Saitoh N, Nagahiro S, Saya H, Nakao M (March 2003). "PML-nuclear bodies are involved in cellular serum response". Genes Cells. 8 (3): 275–86. doi:10.1046/j.1365-2443.2003.00632.x. PMID 12622724.
  17. ↑ Hassler M, Richmond TJ (June 2001). "The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex". EMBO J. 20 (12): 3018–28. doi:10.1093/emboj/20.12.3018. PMC 150215. PMID 11406578.
  18. ↑ Belaguli NS, Sepulveda JL, Nigam V, Charron F, Nemer M, Schwartz RJ (October 2000). "Cardiac tissue enriched factors serum response factor and GATA-4 are mutual coregulators". Mol. Cell. Biol. 20 (20): 7550–8. doi:10.1128/mcb.20.20.7550-7558.2000. PMC 86307. PMID 11003651.
  19. ↑ Morin S, Paradis P, Aries A, Nemer M (February 2001). "Serum response factor-GATA ternary complex required for nuclear signaling by a G-protein-coupled receptor". Mol. Cell. Biol. 21 (4): 1036–44. doi:10.1128/MCB.21.4.1036-1044.2001. PMC 99558. PMID 11158291.
  20. ↑ Joliot V, Demma M, Prywes R (February 1995). "Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor". Nature. 373 (6515): 632–5. doi:10.1038/373632a0. PMID 7854423.
  21. ↑ Zhu H, Joliot V, Prywes R (February 1994). "Role of transcription factor TFIIF in serum response factor-activated transcription". J. Biol. Chem. 269 (5): 3489–97. PMID 8106390.
  22. ↑ Grueneberg DA, Henry RW, Brauer A, Novina CD, Cheriyath V, Roy AL, Gilman M (October 1997). "A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I". Genes Dev. 11 (19): 2482–93. doi:10.1101/gad.11.19.2482. PMC 316568. PMID 9334314.
  23. ↑ Kim DW, Cheriyath V, Roy AL, Cochran BH (June 1998). "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Mol. Cell. Biol. 18 (6): 3310–20. doi:10.1128/mcb.18.6.3310. PMC 108912. PMID 9584171.
  24. ↑ Groisman R, Masutani H, Leibovitch MP, Robin P, Soudant I, Trouche D, Harel-Bellan A (March 1996). "Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins". J. Biol. Chem. 271 (9): 5258–64. doi:10.1074/jbc.271.9.5258. PMID 8617811.
  25. ↑ Biesiada E, Hamamori Y, Kedes L, Sartorelli V (April 1999). "Myogenic basic helix-loop-helix proteins and Sp1 interact as components of a multiprotein transcriptional complex required for activity of the human cardiac alpha-actin promoter". Mol. Cell. Biol. 19 (4): 2577–84. PMC 84050. PMID 10082523.
  26. ↑ Yamada K, Osawa H, Granner DK (October 1999). "Identification of proteins that interact with NF-YA". FEBS Lett. 460 (1): 41–5. doi:10.1016/s0014-5793(99)01311-3. PMID 10571058.
  27. ↑ Lee SK, Kim JH, Lee YC, Cheong J, Lee JW (April 2000). "Silencing mediator of retinoic acid and thyroid hormone receptors, as a novel transcriptional corepressor molecule of activating protein-1, nuclear factor-kappaB, and serum response factor". J. Biol. Chem. 275 (17): 12470–4. doi:10.1074/jbc.275.17.12470. PMID 10777532.
  28. ↑ Kim HJ, Kim JH, Lee JW (October 1998). "Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations". J. Biol. Chem. 273 (44): 28564–7. doi:10.1074/jbc.273.44.28564. PMID 9786846.
  29. ↑ Gupta M, Kogut P, Davis FJ, Belaguli NS, Schwartz RJ, Gupta MP (March 2001). "Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1". J. Biol. Chem. 276 (13): 10413–22. doi:10.1074/jbc.M008625200. PMID 11136726.
  30. ↑ Koegel H, von Tobel L, Schäfer M, Alberti S, Kremmer E, Mauch C, Hohl D, Wang XJ, Beer HD, Bloch W, Nordheim A, Werner S (April 2009). "Loss of serum response factor in keratinocytes results in hyperproliferative skin disease in mice". J. Clin. Invest. 119 (4): 899–910. doi:10.1172/JCI37771. PMC 2662566. PMID 19307725.

Acknowledgements

Initial content for this page in some instances incorporates text from the United States National Library of Medicine.

External links

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